NPBL_COPC7
ID NPBL_COPC7 Reviewed; 2072 AA.
AC Q00333; A8NQY8;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Protein rad9;
DE AltName: Full=SCC2 homolog;
GN Name=rad9; ORFNames=CC1G_03361;
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RX PubMed=8846891; DOI=10.1093/genetics/142.4.1105;
RA Seitz L.C., Tang K., Cummings W.J., Zolan M.E.;
RT "The rad9 gene of Coprinus cinereus encodes a proline-rich protein required
RT for meiotic chromosome condensation and synapsis.";
RL Genetics 142:1105-1117(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
RN [3]
RP FUNCTION.
RX PubMed=12407179; DOI=10.1073/pnas.232316999;
RA Cummings W.J., Merino S.T., Young K.G., Li L., Johnson C.W., Sierra E.A.,
RA Zolan M.E.;
RT "The Coprinus cinereus adherin Rad9 functions in Mre11-dependent DNA
RT repair, meiotic sister-chromatid cohesion, and meiotic homolog pairing.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14958-14963(2002).
CC -!- FUNCTION: Plays a structural role in chromatin. Involved in sister
CC chromatid cohesion during meiosis, possibly by interacting with the
CC cohesin complex. Also participates in DNA repair and meiotic homolog
CC pairing. {ECO:0000269|PubMed:12407179, ECO:0000269|PubMed:8846891}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed during meiosis.
CC {ECO:0000269|PubMed:8846891}.
CC -!- INDUCTION: Following irradiation. {ECO:0000269|PubMed:8846891}.
CC -!- SIMILARITY: Belongs to the SCC2/Nipped-B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC49309.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=EAU86150.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U34998; AAC49309.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AACS02000008; EAU86150.2; ALT_SEQ; Genomic_DNA.
DR PIR; S71461; S71461.
DR RefSeq; XP_001835579.2; XM_001835527.2.
DR AlphaFoldDB; Q00333; -.
DR SMR; Q00333; -.
DR STRING; 5346.XP_001835579.2; -.
DR EnsemblFungi; EAU86150; EAU86150; CC1G_03361.
DR GeneID; 6012112; -.
DR KEGG; cci:CC1G_03361; -.
DR eggNOG; KOG1020; Eukaryota.
DR HOGENOM; CLU_000655_0_0_1; -.
DR InParanoid; Q00333; -.
DR OrthoDB; 608077at2759; -.
DR Proteomes; UP000001861; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0061780; P:mitotic cohesin loading; IEA:InterPro.
DR GO; GO:0010468; P:regulation of gene expression; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR026003; Cohesin_HEAT.
DR InterPro; IPR024986; Nipped-B_C.
DR InterPro; IPR033031; Scc2/Nipped-B.
DR PANTHER; PTHR21704; PTHR21704; 1.
DR Pfam; PF12765; Cohesin_HEAT; 1.
DR Pfam; PF12830; Nipped-B_C; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; DNA damage; DNA repair; Meiosis; Nucleus; Reference proteome;
KW Repeat.
FT CHAIN 1..2072
FT /note="Protein rad9"
FT /id="PRO_0000218600"
FT REPEAT 882..919
FT /note="HEAT 1"
FT REPEAT 1203..1240
FT /note="HEAT 2"
FT REPEAT 1242..1279
FT /note="HEAT 3"
FT REPEAT 1318..1355
FT /note="HEAT 4"
FT REPEAT 1734..1772
FT /note="HEAT 5"
FT REPEAT 1858..1896
FT /note="HEAT 6"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..259
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..324
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 389
FT /note="P -> A (in Ref. 1; AAC49309)"
FT /evidence="ECO:0000305"
FT CONFLICT 814..819
FT /note="KKEKES -> EREKREN (in Ref. 1; AAC49309)"
FT /evidence="ECO:0000305"
FT CONFLICT 974
FT /note="K -> R (in Ref. 1; AAC49309)"
FT /evidence="ECO:0000305"
FT CONFLICT 1018
FT /note="K -> M (in Ref. 1; AAC49309)"
FT /evidence="ECO:0000305"
FT CONFLICT 1127
FT /note="A -> G (in Ref. 1; AAC49309)"
FT /evidence="ECO:0000305"
FT CONFLICT 1159
FT /note="Q -> L (in Ref. 1; AAC49309)"
FT /evidence="ECO:0000305"
FT CONFLICT 1167
FT /note="E -> G (in Ref. 1; AAC49309)"
FT /evidence="ECO:0000305"
FT CONFLICT 1178
FT /note="D -> G (in Ref. 1; AAC49309)"
FT /evidence="ECO:0000305"
FT CONFLICT 1317
FT /note="T -> A (in Ref. 1; AAC49309)"
FT /evidence="ECO:0000305"
FT CONFLICT 1359
FT /note="A -> G (in Ref. 1; AAC49309)"
FT /evidence="ECO:0000305"
FT CONFLICT 1412
FT /note="N -> D (in Ref. 1; AAC49309)"
FT /evidence="ECO:0000305"
FT CONFLICT 1773
FT /note="P -> T (in Ref. 1; AAC49309)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2072 AA; 229232 MW; 4086DB3D98AFEAE1 CRC64;
MDHNSNHHWY SQNRPRNDPR IPSQQSPNTN INHHGFTNAA NQTVQHAQQM LAGFPMASAT
PALQPVRHIA NMTMTAAPPS FVQPNYYSSQ AQPDYTHVQQ HNSQHIPPPP YTEYDQHLSY
LSAPQVPQNR TEHWHTARDQ SVRLLNEQAS RSYPYQEPQQ PSNWPASSYQ STPFAQSVFQ
RTTPNSAYPT PPPPGISTSS SSLAFALGGP PQPPPRQQTV TQPLFHPTQA PLPQPAPAPQ
PAPVPQATVF PPPSNPPAAQ ASQPTYNADD SASFFNSFLE RKTREMNATM QQTTSAKSIF
PPAPAKLPLP VPVASKPPAR MKTPPPREQK AVPDSSPDPL SLSSNMALPS STPLKRKCVV
EIHSPPPKRI QSYKPMTLIS QPLTPSRGPP LTPTSRASNA SSVPTTASSS TSITSMSSSS
KTTVPMTPTP QRIGRKYEDT PDLGGYGSSE DTPLRRGLMS SVKRTGERDD RGPLEKFVTV
VDEIFESEDS LPADLGHEDL PQEFFSSWSP DCSKPLLNTS TIRKLLKYVG QVARPTKRMR
QASAGGQGLL ATPRTRAGRM ADVDIQTLSR LLKMLERSLK EGEEVDPFKA TGSSSGLNGT
VSARSSPVKK GSRKKKAKDS LDDDDSMEAD EADELPQQHL KKGSTPPPND IELEKLTRLL
DLARDSVLAA DCCIAILASD RLPKQLYSEE LITSCLNTVK NQLTKVLYPF IEGASPDSIN
SKLYNGALLQ HLIKNAPADP NTSANSSISQ AYHRKQMSEI FQSLSSVLPR INALANAESV
AMSDSIIIQT VYIAIGPFFV VEGAEESTAK SASKKEKESV VNRTLGKSAM RGLRLDALSL
IRSIFSNHED QRSWIIEEIL TSLIKLSDTK QKAGQFRLRD GRSIRTVSAL LMQLVQTSAH
DVRINARRLE KERQNALALK RQESISDLNG QPKSDEPFLD NIDMEEIRLY GGGLESATKA
AKTIIFFLNS RAGKGKTTKN SNEAEYRAIF DNLIDDLLVV LYWPEWPAAS LLLNIASKFM
VSSLDDVKSN AQIDTNAAKS MALDHLGVIA ARIRSSILKV QKDEDGTSYR GLKPLDEIVN
NLQSKQFAKF MDAHRDVAAH LCKRSTEDQA YESARELTAA ILGHELAASL KRVNVWLDHP
EQDEDLDLRD SSKALSFGQK LKTALREVWK DPATDVFDIG SQEEVSRIDR LSEEIGTIQS
LRNSFQPILN VILSALDAPV IFMRTKALRA LGQIVTSDAT ILGTASVRQG IENHLLDSSP
AVRDAAVELI GKYMIDSPEV AGNYYQKIAE RMADTGLAVR KRVIKLLKSY YGVIDDTQRK
IDISARLVLR MVDEDDGVKD LAMKTLEELW FPPLPPPSAM KVKPTSSSNP NQDKAALLSK
VAIIMGTAAN FRDRQSPLED MLHKIISDKE GNEAASLHQR YAEICETLID GLVDATDLPG
FTIINCIRTI HLFTAAYPSI LPGTHASTLL PYLKNASTTE ELLTSDFLLK IFRASIPHMP
KTAAKFGQEL QTSLQPLILK PFGGVNILQE AVGCMCAVVR HLTHDFKRLI NLLKGCNARL
LSYLRHPPTK QLNNVESKTL LMLLFIVALL GEHCNFDRLR LEQPDLAPDI DSITQGSVME
HIYFTLLRIY DKFDFADIRP RILQCLGFLF RAQPTLMTKE ESAAIMDAIF ASEEEEGRAR
LLKIMQDFLI SESEKHSAKE KESAKNKNKA NTDVNMEELV GNTDGFADSG VSSAIVQRYL
SHILDAALSQ NSQIQMAAID VLTFTIKQGL AHPLQSFPVI IALETSPHAV LSARAIALHS
ILNSKHASLL NTRYSISARK SFDYQKKIVD GVVHGFRTNG HPTALLQRWY TLVREKRATR
QDFLKSLVKV FSENDSYQAT QDDVDFTRYM AENFASFEYK TQEEVFTVIK HLTTVLSTTG
MQLLDIISPA HLLSQIQPSH SQPSQHNGGD EISSNAAEAV VPLATPNYGD RDPVSLMRTS
VIVAMVMLLK SYLKTLYGLS EDKCNKFVIG KKSAIGDRPA TKRSDKPISW EKLPYAVQAI
HTTQDVELQK QRFLEIWNED GVTAEPEDDE FL
